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    Echelon Biosciences ptdins 3 5 p 2 dic8
    a , Sample traces and current density (current/capacitance) of the wild type and L11A/I12A mutant of MmTPC1 recorded in the whole cell configuration with 100 μM PtdIns(3,5)P 2 in the pipette (cytosolic). The experiments were repeated five times independently with similar results. Data points for current density are mean ± SEM (n=5 independent experiments). L11A/I12A mutant elicited much larger whole cell currents and therefore was used as the wild type channel in all our recordings. The extracellular side of MmTPC1 in plasma membrane is equivalent to the luminal side of MmTPC1 in lysosomes. b , Sample traces of PtdIns(3,5)P 2 -dependent voltage activation of MmTPC1. Whole cell currents were recorded with varying PtdIns(3,5)P 2 concentrations in the pipette (cytosolic) at pH 7.4. The experiments were repeated five times independently with similar results. c , G/G max -V curves of MmTPC1 at various PtdIns(3,5)P 2 concentrations. Boltzmann fit yields V 1/2 (mV)= 21.6 ± 1.2, 15.2 ± 1.0, 16.1 ± 0.9, −2.0 ± 1.0 and Z=0.78 ± 0.04, 0.82 ± 0.03, 0.89 ± 0.02, 0.84 ± 0.05 for voltage activation in 0.05, 0.2, 2.0, 10 μM cytosolic PtdIns(3,5)P 2 , respectively, where V 1/2 is the membrane potential for half maximum activation and Z is apparent valence. All data points are mean ± SEM (n=5 independent experiments). d , Luminal pH modulates the voltage activation of MmTPC1. Whole cell currents of MmTPC1 recorded in the presence of 2 μM cytosolic PtdIns(3,5)P 2 with varying luminal (bath) pH of 7.4, 6.0 or 4.6. Sample traces were obtained from the same patch. The experiments were repeated five times independently with similar results. e , G/G max -V curves of MmTPC1 at various luminal pH. Boltzmann fit yields V 1/2 = 16.2 ± 0.8 mV, Z= 0.91 ± 0.02 at pH 7.4, V 1/2 = 38.2 ± 1.2 mV, Z=0.95 ± 0.02 at pH 6.0. All data points were normalized against G max obtained at 100 mV activation voltage and pH 7.4. All data points are mean ± SEM (n=5 independent experiments). f , Sample traces of whole cell currents with 150 mM Na + in the pipette solution and 150 mM X (X=150 mM Na + or 145 mM K + and 5 mM Na + ) in the bath solution, and the I–V curves generated from the tail currents of the sample traces. g , Sample traces of whole cell currents with 150 mM Na + in the pipette solution and 150 mM Na + or 100 mM Ca 2+ in the bath solution, and the I–V curves generated from the tail currents of the sample traces. Data in ( f ) and ( g ) were recorded with 10 μM PtdIns(3,5)P 2 in the pipette at pH 7.4 and both experiments were repeated five times independently with similar results.
    Ptdins 3 5 P 2 Dic8, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Structural insights into the voltage and phospholipid activation of mammalian TPC1 channel"

    Article Title: Structural insights into the voltage and phospholipid activation of mammalian TPC1 channel

    Journal: Nature

    doi: 10.1038/nature26139

    a , Sample traces and current density (current/capacitance) of the wild type and L11A/I12A mutant of MmTPC1 recorded in the whole cell configuration with 100 μM PtdIns(3,5)P 2 in the pipette (cytosolic). The experiments were repeated five times independently with similar results. Data points for current density are mean ± SEM (n=5 independent experiments). L11A/I12A mutant elicited much larger whole cell currents and therefore was used as the wild type channel in all our recordings. The extracellular side of MmTPC1 in plasma membrane is equivalent to the luminal side of MmTPC1 in lysosomes. b , Sample traces of PtdIns(3,5)P 2 -dependent voltage activation of MmTPC1. Whole cell currents were recorded with varying PtdIns(3,5)P 2 concentrations in the pipette (cytosolic) at pH 7.4. The experiments were repeated five times independently with similar results. c , G/G max -V curves of MmTPC1 at various PtdIns(3,5)P 2 concentrations. Boltzmann fit yields V 1/2 (mV)= 21.6 ± 1.2, 15.2 ± 1.0, 16.1 ± 0.9, −2.0 ± 1.0 and Z=0.78 ± 0.04, 0.82 ± 0.03, 0.89 ± 0.02, 0.84 ± 0.05 for voltage activation in 0.05, 0.2, 2.0, 10 μM cytosolic PtdIns(3,5)P 2 , respectively, where V 1/2 is the membrane potential for half maximum activation and Z is apparent valence. All data points are mean ± SEM (n=5 independent experiments). d , Luminal pH modulates the voltage activation of MmTPC1. Whole cell currents of MmTPC1 recorded in the presence of 2 μM cytosolic PtdIns(3,5)P 2 with varying luminal (bath) pH of 7.4, 6.0 or 4.6. Sample traces were obtained from the same patch. The experiments were repeated five times independently with similar results. e , G/G max -V curves of MmTPC1 at various luminal pH. Boltzmann fit yields V 1/2 = 16.2 ± 0.8 mV, Z= 0.91 ± 0.02 at pH 7.4, V 1/2 = 38.2 ± 1.2 mV, Z=0.95 ± 0.02 at pH 6.0. All data points were normalized against G max obtained at 100 mV activation voltage and pH 7.4. All data points are mean ± SEM (n=5 independent experiments). f , Sample traces of whole cell currents with 150 mM Na + in the pipette solution and 150 mM X (X=150 mM Na + or 145 mM K + and 5 mM Na + ) in the bath solution, and the I–V curves generated from the tail currents of the sample traces. g , Sample traces of whole cell currents with 150 mM Na + in the pipette solution and 150 mM Na + or 100 mM Ca 2+ in the bath solution, and the I–V curves generated from the tail currents of the sample traces. Data in ( f ) and ( g ) were recorded with 10 μM PtdIns(3,5)P 2 in the pipette at pH 7.4 and both experiments were repeated five times independently with similar results.
    Figure Legend Snippet: a , Sample traces and current density (current/capacitance) of the wild type and L11A/I12A mutant of MmTPC1 recorded in the whole cell configuration with 100 μM PtdIns(3,5)P 2 in the pipette (cytosolic). The experiments were repeated five times independently with similar results. Data points for current density are mean ± SEM (n=5 independent experiments). L11A/I12A mutant elicited much larger whole cell currents and therefore was used as the wild type channel in all our recordings. The extracellular side of MmTPC1 in plasma membrane is equivalent to the luminal side of MmTPC1 in lysosomes. b , Sample traces of PtdIns(3,5)P 2 -dependent voltage activation of MmTPC1. Whole cell currents were recorded with varying PtdIns(3,5)P 2 concentrations in the pipette (cytosolic) at pH 7.4. The experiments were repeated five times independently with similar results. c , G/G max -V curves of MmTPC1 at various PtdIns(3,5)P 2 concentrations. Boltzmann fit yields V 1/2 (mV)= 21.6 ± 1.2, 15.2 ± 1.0, 16.1 ± 0.9, −2.0 ± 1.0 and Z=0.78 ± 0.04, 0.82 ± 0.03, 0.89 ± 0.02, 0.84 ± 0.05 for voltage activation in 0.05, 0.2, 2.0, 10 μM cytosolic PtdIns(3,5)P 2 , respectively, where V 1/2 is the membrane potential for half maximum activation and Z is apparent valence. All data points are mean ± SEM (n=5 independent experiments). d , Luminal pH modulates the voltage activation of MmTPC1. Whole cell currents of MmTPC1 recorded in the presence of 2 μM cytosolic PtdIns(3,5)P 2 with varying luminal (bath) pH of 7.4, 6.0 or 4.6. Sample traces were obtained from the same patch. The experiments were repeated five times independently with similar results. e , G/G max -V curves of MmTPC1 at various luminal pH. Boltzmann fit yields V 1/2 = 16.2 ± 0.8 mV, Z= 0.91 ± 0.02 at pH 7.4, V 1/2 = 38.2 ± 1.2 mV, Z=0.95 ± 0.02 at pH 6.0. All data points were normalized against G max obtained at 100 mV activation voltage and pH 7.4. All data points are mean ± SEM (n=5 independent experiments). f , Sample traces of whole cell currents with 150 mM Na + in the pipette solution and 150 mM X (X=150 mM Na + or 145 mM K + and 5 mM Na + ) in the bath solution, and the I–V curves generated from the tail currents of the sample traces. g , Sample traces of whole cell currents with 150 mM Na + in the pipette solution and 150 mM Na + or 100 mM Ca 2+ in the bath solution, and the I–V curves generated from the tail currents of the sample traces. Data in ( f ) and ( g ) were recorded with 10 μM PtdIns(3,5)P 2 in the pipette at pH 7.4 and both experiments were repeated five times independently with similar results.

    Techniques Used: Mutagenesis, Transferring, Activation Assay, Generated

    a, 3D reconstruction of PtdIns(3,5)P 2 -bound (purple density) MmTPC1 dimer with each subunit in individual color. b , Cartoon representation of MmTPC1 in the same orientations as the EM maps in a . N-acetylglucosamine (NAG) molecules and PtdIns(3,5)P 2 are shown as sticks. c , Topology and domain arrangement of MmTPC1 subunit. d , Structure of the 6-TM I and the soluble domain with individual element colored as that in c . Inset: zoomed-in view of the cytosolic soluble domain. e , Structure of the 6-TM II.
    Figure Legend Snippet: a, 3D reconstruction of PtdIns(3,5)P 2 -bound (purple density) MmTPC1 dimer with each subunit in individual color. b , Cartoon representation of MmTPC1 in the same orientations as the EM maps in a . N-acetylglucosamine (NAG) molecules and PtdIns(3,5)P 2 are shown as sticks. c , Topology and domain arrangement of MmTPC1 subunit. d , Structure of the 6-TM I and the soluble domain with individual element colored as that in c . Inset: zoomed-in view of the cytosolic soluble domain. e , Structure of the 6-TM II.

    Techniques Used:

    a, Partial S4 sequence alignment and arginine registry. b , Side view of VSD1 with IS1 omitted for clarity. c , G/G max -V curves of wild-type MmTPC1 and IS4 arginine mutations. Sample traces are shown in  . All data points are mean ± SEM (n=5 independent experiments). d , Side view of VSD2 with IIS1 omitted for clarity. e , Sample I–V curves of wild-type MmTPC1 (obtained from the peak currents at various activation potentials) and Arg540Gln mutant (obtained by applying voltage pulses ramp from −100 to +100 mV). Currents were recorded with 2 μM PtdIns(3,5)P 2 in the pipette and repeated five times independently with similar results. f , Structural comparison of VSD2 between the PtdIns(3,5)P 2 -bound MmTPC1 (orange) and AtTPC1 (cyan) with S1 helices omitted for clarity. g , Cartoon representation of VSD2 conformational change from the activated to resting state. Red arrows indicate the concurrent movements of S4 and S4–S5 linker.
    Figure Legend Snippet: a, Partial S4 sequence alignment and arginine registry. b , Side view of VSD1 with IS1 omitted for clarity. c , G/G max -V curves of wild-type MmTPC1 and IS4 arginine mutations. Sample traces are shown in . All data points are mean ± SEM (n=5 independent experiments). d , Side view of VSD2 with IIS1 omitted for clarity. e , Sample I–V curves of wild-type MmTPC1 (obtained from the peak currents at various activation potentials) and Arg540Gln mutant (obtained by applying voltage pulses ramp from −100 to +100 mV). Currents were recorded with 2 μM PtdIns(3,5)P 2 in the pipette and repeated five times independently with similar results. f , Structural comparison of VSD2 between the PtdIns(3,5)P 2 -bound MmTPC1 (orange) and AtTPC1 (cyan) with S1 helices omitted for clarity. g , Cartoon representation of VSD2 conformational change from the activated to resting state. Red arrows indicate the concurrent movements of S4 and S4–S5 linker.

    Techniques Used: Sequencing, Activation Assay, Mutagenesis, Transferring


    Figure Legend Snippet: Cryo-EM data collection and model statistics.

    Techniques Used:

    ptdins 3 5 p 2  (Echelon Biosciences)


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